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Q9JIF5

- PECR_CAVPO

UniProt

Q9JIF5 - PECR_CAVPO

Protein

Peroxisomal trans-2-enoyl-CoA reductase

Gene

PECR

Organism
Cavia porcellus (Guinea pig)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Participates in chain elongation of fatty acids. Has no 2,4-dienoyl-CoA reductase activity.

    Catalytic activityi

    Acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH.1 Publication

    Kineticsi

    1. KM=11 µM for decenoyl-CoA1 Publication
    2. KM=53 µM for NADPH1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei178 – 1781Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi23 – 4725NADPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. trans-2-enoyl-CoA reductase (NADPH) activity Source: UniProtKB

    GO - Biological processi

    1. fatty acid biosynthetic process Source: UniProtKB-UniPathway
    2. phytol metabolic process Source: Ensembl

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    SABIO-RKQ9JIF5.
    UniPathwayiUPA00094.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxisomal trans-2-enoyl-CoA reductase (EC:1.3.1.38)
    Gene namesi
    Name:PECR
    OrganismiCavia porcellus (Guinea pig)
    Taxonomic identifieri10141 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia
    ProteomesiUP000005447: Unplaced

    Subcellular locationi

    Peroxisome 1 Publication

    GO - Cellular componenti

    1. intracellular membrane-bounded organelle Source: UniProtKB
    2. mitochondrion Source: UniProtKB
    3. peroxisomal membrane Source: UniProtKB

    Keywords - Cellular componenti

    Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 302301Peroxisomal trans-2-enoyl-CoA reductasePRO_0000054739Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylglycineBy similarity
    Modified residuei32 – 321N6-succinyllysineBy similarity
    Modified residuei83 – 831N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Expressioni

    Tissue specificityi

    Expressed in liver.1 Publication

    Interactioni

    Subunit structurei

    Interacts with PEX5, probably required to target it into peroxisomes.By similarity

    Protein-protein interaction databases

    STRINGi10141.ENSCPOP00000010538.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JIF5.
    SMRiQ9JIF5. Positions 8-302.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi300 – 3023Microbody targeting signalBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1028.
    GeneTreeiENSGT00740000115347.
    HOVERGENiHBG105268.
    InParanoidiQ9JIF5.
    OMAiNISSRAW.
    OrthoDBiEOG7Q5HFK.
    TreeFamiTF315256.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PRINTSiPR00081. GDHRDH.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9JIF5-1 [UniParc]FASTAAdd to Basket

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    MGSWTKCQSC LAPGLLQNRA AIVTGGGTGI GKAIAKELLH LGCNVVIASR    50
    KFDRLRAAAE ELKATLPPSN KAEVTPIQCN IRKEEEVNNL MKSTLALYGK 100
    IDFLVNNGGG QFWSSPEHIS SKGWHAVIET NLTGTFYMCK AAYNSWMKEH 150
    GGAIVNIIIL LNGQPFVAHS GAARGGVYNL TKSLALGWAR SGIRINCVAP 200
    GTVYSQTAMD NYGDMGKTLF ADAFQKIPAK RLGVPEEVSS LVCFLLSPAA 250
    SFITGQLVNV DGGQSLYCQN HDIPDHDNWP EGVGDLSTVK KMKESFKQKA 300
    KL 302
    Length:302
    Mass (Da):32,529
    Last modified:October 1, 2000 - v1
    Checksum:i9C1430D90D4C07C2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF232010 mRNA. Translation: AAF69799.1.
    RefSeqiXP_003462124.1. XM_003462076.2.

    Genome annotation databases

    EnsembliENSCPOT00000011831; ENSCPOP00000010538; ENSCPOG00000011717.
    GeneIDi100725791.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF232010 mRNA. Translation: AAF69799.1 .
    RefSeqi XP_003462124.1. XM_003462076.2.

    3D structure databases

    ProteinModelPortali Q9JIF5.
    SMRi Q9JIF5. Positions 8-302.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10141.ENSCPOP00000010538.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSCPOT00000011831 ; ENSCPOP00000010538 ; ENSCPOG00000011717 .
    GeneIDi 100725791.

    Organism-specific databases

    CTDi 55825.

    Phylogenomic databases

    eggNOGi COG1028.
    GeneTreei ENSGT00740000115347.
    HOVERGENi HBG105268.
    InParanoidi Q9JIF5.
    OMAi NISSRAW.
    OrthoDBi EOG7Q5HFK.
    TreeFami TF315256.

    Enzyme and pathway databases

    UniPathwayi UPA00094 .
    SABIO-RK Q9JIF5.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PRINTSi PR00081. GDHRDH.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and expression of mammalian peroxisomal trans-2-enoyl-coenzyme A reductase cDNAs."
      Das A.K., Uhler M.D., Hajra A.K.
      J. Biol. Chem. 275:24333-24340(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 92-118, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Liver.

    Entry informationi

    Entry nameiPECR_CAVPO
    AccessioniPrimary (citable) accession number: Q9JIF5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 77 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3